Reviewed, UniProtKB/Swiss-Prot P15651 (ACADS_RAT)

Names and origin

Protein names

Recommended name:
    Short-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=SCAD
    EC=1.3.99.2
Alternative name(s):
    Butyryl-CoA dehydrogenase

Gene names

Name:

Acads

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor.
Cofactor	FAD.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer. Ref.2
Subcellular location	Mitochondrion matrix.
Miscellaneous	A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.2 Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to starvation Inferred from expression pattern. Source: RGD
Cellular component	mitochondrial matrix Ref.2 Traceable author statement. Source: RGD
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA binding Inferred from direct assay. Source: RGD butyryl-CoA dehydrogenase activity Ref.2 Inferred from direct assay. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

24

Mitochondrion

Chain

25 – 412

388

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000501

Regions

Nucleotide binding

152 – 161

10

FAD

Nucleotide binding

185 – 187

3

FAD

Nucleotide binding

365 – 369

5

FAD

Nucleotide binding

394 – 396

3

FAD

Region

269 – 272

4

Substrate binding

Region

392 – 393

2

Substrate binding

Sites

Active site

392

1

Proton acceptor

Binding site

161

1

Substrate; via carbonyl oxygen

Binding site

297

1

FAD

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

412

Helix Strand Turn

Details...

Helix

36 – 52

17

Turn

53 – 56

4

Helix

57 – 63

7

Helix

68 – 77

10

Turn

78 – 80

3

Beta strand

81 – 84

4

Helix

86 – 88

3

Helix

95 – 108

14

Helix

110 – 121

12

Helix

124 – 130

7

Helix

133 – 139

7

Helix

141 – 143

3

Beta strand

144 – 147

4

Beta strand

150 – 153

4

Beta strand

159 – 162

4

Beta strand

169 – 172

4

Beta strand

174 – 187

14

Turn

188 – 191

4

Beta strand

193 – 201

9

Helix

203 – 208

6

Beta strand

209 – 218

10

Beta strand

222 – 224

3

Beta strand

230 – 232

3

Beta strand

238 – 249

12

Helix

250 – 252

3

Beta strand

253 – 256

4

Helix

260 – 296

37

Beta strand

298 – 303

6

Helix

304 – 306

3

Helix

308 – 336

29

Helix

342 – 367

26

Helix

368 – 371

4

Helix

378 – 385

8

Helix

386 – 389

4

Turn

390 – 392

3

Helix

395 – 410

16

Sequences

	Sequence		Length	Mass (Da)
	P15651-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 3E4A052FC99B8E14	FASTA	412	44,765
	10 20 30 40 50 60 MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL 70 80 90 100 110 120 DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRGCA STGVIMSVNN 130 140 150 160 170 180 SLYLGPILKF GSSQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN 190 200 210 220 230 240 GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN 250 260 270 280 290 300 LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF 310 320 330 340 350 360 GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS 370 380 390 400 410 HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS

References

[1]

"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family." Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K. J. Biol. Chem. 264:16321-16331(1989) [PubMed: 2777793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

[2]

"Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases." Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., Kim J.-J.P. J. Biol. Chem. 277:12200-12207(2002) [PubMed: 11812788] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 27-412 IN COMPLEX WITH ACETOACETYL-COA AND FAD, HOMOTETRAMERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05030 mRNA. Translation: AAA40669.1. Different initiation.

IPI

IPI00231359.

PIR

B34252.

RefSeq

NP_071957.1.

UniGene

Rn.1167

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JQI	X-ray	2.25	A/B	25-412	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSRNOG00000001177. Rattus norvegicus. [Contig view]

GeneID

64304.

KEGG

rno:64304.

Organism-specific databases

RGD

620514. Acads.

Phylogenomic databases

HOVERGEN

P15651.

Enzyme and pathway databases

BRENDA

1.3.99.2. 248.

Gene expression databases

ArrayExpress

P15651.

GermOnline

ENSRNOG00000001177. Rattus norvegicus.

Family and domain databases

InterPro

IPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]

Gene3D

G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]

PROSITE

PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

612942.

Entry information

Entry name

ACADS_RAT

Accession

Primary (citable) accession number: P15651

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)